Peptide structure

Opioid peptides

All peptides are chains of amino acids linked together. A few of these have the ability to affect opioid receptors in the brain and are at the same time difficult to break down. A combination of these two properties leads to protein intolerance in some individuals.

The peptides included in Neurozym's analysis are marked with an asterrisk (*).

Casein peptides

The casomorphines are formed by digestion of the casein protein. The most striking feature in these peptides is the abundance of proline. Casomorphines are known to cause addiction in severe cases of protein intolerance. The length of casomorphins are quite variable.

Rubiscolins are a newly discovered group of opioid peptides. They are formed during digestion of the ribulose bisphosphate carboxylase/oxygenase (Rubisco) protein from spinach leaves. The effects of these peptides on mental health remains unknown.

Opioid peptides may come from other sources than casein, gluten and spinach. Recent research has reveiled opioid peptides also in eggs, oats and rice. We don't have structures for these peptides yet.

In addition, there is a peptide which is called dermorphin. Dermorphin is from a microbial source, but the organism(s) responsible remains elusive. It has a D-Alanin residue, which is not known in higher organisms. The guess is that dermorphin is produced by bacteria or molds. Deltorphin I and II are quite similar in structure and are from fungal sources.